title: D-Malate dehydrogenase from Pseudomonas fluorescens UK-1.
abstract: An enzyme catalyzing oxidative decarboxylation of D-malate was induced by D-malate and beta, beta-dimethyl-malate in Pseudomonas fluorescens UK-1. D-Malate dehydrogenase was purified to homogeneity from the cells grown on D-malate by using ammonium sulfate precipitation, heat treatment, DEAE-sephadex chromatography, Ultrogel AcA 34 gel filtration and 5'-AMP-Sepharose affinity chromatography. D-Malate dehydrogenase has a molecular weight of 140 000 and contains 4 identical subunits of 34 000. The enzyme is very stable against sulfhydryl group reagents or alkylating agents and rather stable against heat or protein denaturants like urea or sodium dodecyl sulfate. NAD protects against heat inactivation and trypsinization but not against protein denaturants. D-Malate dehydrogenase from Escherichia coli does not cross-react with anti-D-malate dehydrogenase to D-malate dehydrogenase form P.fluorescens UK-1.
mesh_terms: D007120:Immunochemistry; D008291:Malate Dehydrogenase / Q000378:metabolism*; D008970:Molecular Weight; D011551:Pseudomonas fluorescens / Q000201:enzymology*
chemical_list: D008291:Malate Dehydrogenase